Type III Effector NleH2 from Escherichia coli O157:H7 str. Sakai Features an Atypical Protein Kinase Domain

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• 作者：Andrei S. Halavaty ; Spencer M. Anderson ; Zdzislaw Wawrzak ; Marina Kudritska ; Tatiana Skarina ; Wayne F. Anderson ; Alexei Savchenko
• 刊名：Biochemistry
• 出版年：2014
• 出版时间：April 22, 2014
• 年：2014
• 卷：53
• 期：15
• 页码：2433-2435
• 全文大小：218K
• 年卷期：v.53,no.15(April 22, 2014)
• ISSN：1520-4995

文摘

The crystal structure of a C-terminal domain of enterohemorrhagic Escherichia coli type III effector NleH2 has been determined to 2.6 脜 resolution. The structure resembles those of protein kinases featuring the catalytic, activation, and glycine-rich loop motifs and ATP-binding site. The position of helix 伪C and the lack of a conserved arginine within an equivalent HRD motif suggested that the NleH2 kinase domain鈥檚 active conformation might not require phosphorylation. The activation segment markedly contributed to the dimerization interface of NleH2, which can also accommodate the NleH1鈥揘leH2 heterodimer. The C-terminal PDZ-binding motif of NleH2 provided bases for interaction with host proteins.